REV3L_MOUSE
ID REV3L_MOUSE Reviewed; 3122 AA.
AC Q61493; E9Q1X0; Q9JMD6; Q9QWX6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=DNA polymerase zeta catalytic subunit;
DE EC=2.7.7.7;
DE AltName: Full=Protein reversionless 3-like;
DE Short=REV3-like;
DE AltName: Full=Seizure-related protein 4;
GN Name=Rev3l; Synonyms=Polz, Sez4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129/Ola; TISSUE=Testis;
RX PubMed=10102037; DOI=10.1016/s0921-8777(98)00067-6;
RA van Sloun P.P.H., Romeijn R.J., Eeken J.C.J.;
RT "Molecular cloning, expression and chromosomal localisation of the mouse
RT Rev3l gene, encoding the catalytic subunit of polymerase zeta.";
RL Mutat. Res. 433:109-116(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kajiwara K.;
RT "Molecular analyses of Sez4 encoding murine homologue of yeast REV3 in
RT brain neurons.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2368-3122.
RC STRAIN=C57BL/6J; TISSUE=Embryonic brain;
RX PubMed=8645260; DOI=10.1006/bbrc.1996.0313;
RA Kajiwara K., Nagawawa H., Shimizu-Nishikawa K., Ookura T., Kimura M.,
RA Sugaya E.;
RT "Molecular characterization of seizure-related genes isolated by
RT differential screening.";
RL Biochem. Biophys. Res. Commun. 219:795-799(1996).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1029 AND THR-1040, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalytic subunit of the DNA polymerase zeta complex, an
CC error-prone polymerase specialized in translesion DNA synthesis (TLS).
CC Lacks an intrinsic 3'-5' exonuclease activity and thus has no
CC proofreading function. {ECO:0000250|UniProtKB:O60673}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P14284};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P14284};
CC -!- SUBUNIT: Heterodimer with MAD2L2. This dimer forms the minimal DNA
CC polymerase zeta complex (Pol-zeta2), with REV3L bearing DNA polymerase
CC catalytic activity, although its activity is very low in this context.
CC Component of the tetrameric Pol-zeta complex (Pol-zeta4), which
CC consists of REV3L, MAD2L2, POLD2 and POLD3; Pol-zeta4 is the fully
CC active form of DNA polymerase zeta. {ECO:0000250|UniProtKB:O60673}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DOMAIN: The CysB motif binds 1 4Fe-4S cluster and is required for the
CC formation of polymerase complexes. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
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DR EMBL; AF083464; AAC98785.1; -; mRNA.
DR EMBL; AB031049; BAA90768.1; -; mRNA.
DR EMBL; AC118733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC119943; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; D78644; BAA11461.1; -; mRNA.
DR CCDS; CCDS23790.1; -.
DR PIR; T17202; T17202.
DR RefSeq; NP_035394.2; NM_011264.3.
DR PDB; 4FJO; X-ray; 2.72 A; D=1865-1894.
DR PDBsum; 4FJO; -.
DR SMR; Q61493; -.
DR BioGRID; 202866; 6.
DR STRING; 10090.ENSMUSP00000019986; -.
DR iPTMnet; Q61493; -.
DR PhosphoSitePlus; Q61493; -.
DR EPD; Q61493; -.
DR jPOST; Q61493; -.
DR MaxQB; Q61493; -.
DR PaxDb; Q61493; -.
DR PeptideAtlas; Q61493; -.
DR PRIDE; Q61493; -.
DR ProteomicsDB; 253225; -.
DR Antibodypedia; 32376; 105 antibodies from 23 providers.
DR DNASU; 19714; -.
DR Ensembl; ENSMUST00000019986; ENSMUSP00000019986; ENSMUSG00000019841.
DR Ensembl; ENSMUST00000164763; ENSMUSP00000131519; ENSMUSG00000019841.
DR GeneID; 19714; -.
DR KEGG; mmu:19714; -.
DR UCSC; uc007ewc.1; mouse.
DR CTD; 5980; -.
DR MGI; MGI:1337131; Rev3l.
DR VEuPathDB; HostDB:ENSMUSG00000019841; -.
DR eggNOG; KOG0968; Eukaryota.
DR GeneTree; ENSGT00940000156226; -.
DR HOGENOM; CLU_000203_1_0_1; -.
DR InParanoid; Q61493; -.
DR OMA; PVSSCEN; -.
DR OrthoDB; 20210at2759; -.
DR PhylomeDB; Q61493; -.
DR TreeFam; TF101072; -.
DR Reactome; R-MMU-110312; Translesion synthesis by REV1.
DR Reactome; R-MMU-5655862; Translesion synthesis by POLK.
DR Reactome; R-MMU-5656121; Translesion synthesis by POLI.
DR BioGRID-ORCS; 19714; 17 hits in 107 CRISPR screens.
DR ChiTaRS; Rev3l; mouse.
DR PRO; PR:Q61493; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q61493; protein.
DR Bgee; ENSMUSG00000019841; Expressed in ciliary body and 261 other tissues.
DR ExpressionAtlas; Q61493; baseline and differential.
DR Genevisible; Q61493; MM.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016035; C:zeta DNA polymerase complex; ISS:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IMP:MGI.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0042276; P:error-prone translesion synthesis; ISO:MGI.
DR Gene3D; 1.10.132.60; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.90.1600.10; -; 1.
DR InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR032757; DUF4683.
DR InterPro; IPR030559; PolZ_Rev3.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR025687; Znf-C4pol.
DR PANTHER; PTHR45812; PTHR45812; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 2.
DR Pfam; PF15735; DUF4683; 1.
DR Pfam; PF14260; zf-C4pol; 1.
DR PRINTS; PR00106; DNAPOLB.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; DNA damage; DNA repair; DNA replication; DNA-binding;
KW DNA-directed DNA polymerase; Iron; Iron-sulfur; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..3122
FT /note="DNA polymerase zeta catalytic subunit"
FT /id="PRO_0000046469"
FT ZN_FING 3034..3049
FT /note="CysA-type"
FT REGION 270..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1034..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1154..1285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1429..1453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1538..1616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1842..1869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1844..1895
FT /note="Mediates interaction with MAD2L2"
FT /evidence="ECO:0000250"
FT REGION 1959..1979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2091..2138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 3078..3096
FT /note="CysB motif"
FT COMPBIAS 842..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1059
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1178..1194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1240..1268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1538..1557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1571..1585
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1959..1978
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 3034
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 3037
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 3046
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 3049
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 3078
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 3081
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 3091
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 3096
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT MOD_RES 1029
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1040
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1964
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60673"
FT CONFLICT 92
FT /note="G -> A (in Ref. 2; BAA90768)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="A -> T (in Ref. 2; BAA90768)"
FT /evidence="ECO:0000305"
FT CONFLICT 578
FT /note="Q -> E (in Ref. 1; AAC98785)"
FT /evidence="ECO:0000305"
FT CONFLICT 609
FT /note="R -> Q (in Ref. 2; BAA90768)"
FT /evidence="ECO:0000305"
FT CONFLICT 1278
FT /note="P -> L (in Ref. 1; AAC98785)"
FT /evidence="ECO:0000305"
FT CONFLICT 1298
FT /note="F -> L (in Ref. 1; AAC98785)"
FT /evidence="ECO:0000305"
FT CONFLICT 1416
FT /note="P -> L (in Ref. 2; BAA90768)"
FT /evidence="ECO:0000305"
FT CONFLICT 1848
FT /note="T -> A (in Ref. 1; AAC98785)"
FT /evidence="ECO:0000305"
FT CONFLICT 2368
FT /note="V -> G (in Ref. 4; BAA11461)"
FT /evidence="ECO:0000305"
FT CONFLICT 2467
FT /note="A -> G (in Ref. 1; AAC98785, 2; BAA90768 and 4;
FT BAA11461)"
FT /evidence="ECO:0000305"
FT CONFLICT 2883
FT /note="Q -> H (in Ref. 1; AAC98785, 2; BAA90768 and 4;
FT BAA11461)"
FT /evidence="ECO:0000305"
FT HELIX 1870..1873
FT /evidence="ECO:0007829|PDB:4FJO"
FT STRAND 1874..1879
FT /evidence="ECO:0007829|PDB:4FJO"
FT HELIX 1884..1890
FT /evidence="ECO:0007829|PDB:4FJO"
FT HELIX 1891..1893
FT /evidence="ECO:0007829|PDB:4FJO"
SQ SEQUENCE 3122 AA; 350711 MW; 1D365BD1CD5548C2 CRC64;
MFSVRIVTAD YYMASPLPGL DTCQSPLTQL PVKKVPVVRV FGATPAGQKT CLHLHGIFPY
LYVPYDGYGQ QPESYLSQMA FSIDRALNVA LGNPSSTAQH VFKVSLVSGM PFYGYHEKER
HFMKIYLYNP AMVKRICELL QSGAIMNKCY QPHEAHIPYL LQLFIDYNLY GMNLINLAAV
KFRKARRKGN ASHATGLFKH QLSGNSPAGT LFRWEEDEIP SSLLLEGVEP LSTCELEVDA
VAADILNRLD IEAQIGGNPG LQAIWEDEKQ RRRNRNESSQ ISQPESQDCR FVPATESEKQ
FQKRLQEVLK QNDFSVTLSG SVDYSNGSQE FSAELTLHSE ILSPEMLPCS PANMIEVHKD
TDLSKGNTKH KVEEALINEE AILNLIENSQ TFQPLTQRLS ETPVFMGSSP DESLVHLLAG
LESDGYQGEK NRMPLPCHSF GESQNPQNSD DEENEPQIEK EEMELSVVMS QRWDSDIEEH
CAKKRSLCRN AHRSSTEEDD SSSEEEMEWT DNSLLFANLS IPQLDGTADE NSDNPLNNEN
SRAHSSVIAT SKLSVRPSIF HKDAATLEPP SSAKITFQCK HTSALSSHVL NKDGLTEDLS
QPNSTEKGRD NSVTFTKEST YSMKYSGSLS STVHSDNSHK EICKKDKSLP VSSCESSVFD
YEEDIPSVTR QVPSRKYSNM RKIEKDASCI HVNRHISETI LGKNSFNFAD LNHSKRKLSS
EGNEKGNSTS LSGVFPSSLT ENCDLLPSSG ENRSMAHSLE SITDESGLNK LKIRYEEFQE
HKMEKPSLSQ QAAHYMFFPS VVLSNCLTRP QKLSPVTYKL QSGNKPSRLK LNKKKLIGLQ
ETSTKSTETG ATKDSCTHND LYTGASEKEN GLSSDSAKAT HGTFENKPPT EHFIDCHFGD
GSLEAEQSFG LYGNKYTLRA KRKVNYETED SESSFVTQNS KISLPHPMEI GENLDGTLKS
RKRRKMSKKL PPVIIKYIII NRFRGRKNML VKLGKIDSKE KQVILTEEKM ELYKKLAPLK
DFWPKVPDSP ATKYPIYPLT PKKSHRRKSK HKSAKKKPGK QHRTNSENIK RTLSFRKKRT
HAVLSPPSPS YIAETEDCDL SYSDVMSKLG FLSERSTSPI NSSPPRCWSP TDPRAEEIMA
AAEKESMLFK GPNVYNTKTV SPRVGKASRA RAQVKKSKAR LANSSVVTNK RNKRNQTTKL
VDDGKKKPRA KQKQRANEKS LSRKHAIPAD EKMKPHSEAE LTPNHQSVSE LTSSSGAQAL
SKQKEMSQTG PAVDHPLPPA QPTGISAQQR LSNCFSSFLE SKKSVDLRTF PSSRDDSHSS
VVYSSIGPGI SKINIQRSHN QSAMFTRKET TLIQKSIFDL SNHLSQVAQS TQVCSGIISP
KTEESSSTQK NCGSSMGKLN EYRSSLESKP EQVCAPNFLH CKDSQQQTVS VSEQSKTSET
CSPGNAASEE SQTPNCFVTS LKSPIKQIAW EQKQRGFILD MSNFKPEKVK QRSLSEAISQ
TKALSQCKNQ NVSTPSVFGE GQSGLAVLKE LLQKRQQKAQ STNVVQDSTS THQPDKNISV
SNEHKKANKR TRPVTSPRKP RTPRRTKPKE QTPRRLKVDP LNLQTSGHLD NSLSDDSPIL
FSDPGFESCY SLEDSLSPEH NYNFDINTIG QTGFCSFYSG SQFVPADQNL PQKFLSDAVQ
DLFPGQAIDK SELLSHDRQS CSEEKHHVSD SSPWIRASTL NPELFEKVAM DNNENHRHSQ
WKNSFHPLTS HSNSIMESFC VQQAENCLTE KSRLNRSSVS KEVFLSLPQA NSSDWIQGHN
RKEADQSLHS ANTSFTTILS SPDGELVDAA SEDLELYVSR NNDVLTPTPD SSPRSTSSPL
QSKNGSFTPR TAHILKPLMS PPSREEIVAT LLDHDLSEAI YQEPFCSNPS DVPEKPREIG
GRLLMVETRL PNDLIEFEGD FSLEGLRLWK TAFSAMTQNP RPGSPLRNGQ AVVNKESSNS
HKMVEDKKIV IMPCKYAPSR QLVQAWLQAK EEYERSKKLP KTELTPVTKS AENVSPSLNP
GDTCAVSPQV DKCPHTLSSS AHTKEEVSKS QIALQTSTTG CSQTLLAAAS AAVPEEDEDD
NDNCYVSYSS PDSPGIPPWQ QAASPDFRSL NGDDRHSSPG KELCSLAVEN FLKPIKDGIQ
KSSCSESWEP QVISPIHARA RTGKWDPLCL HSTPVMQRKF LEKLPEATGL SPLSVEPKTQ
KLYNKKGSDA DGLRRVLLTT QVENQFAAVN TPKKETSQID GPSLNNTYGF KVSIQNLQEA
KALHEIQNLT LISVELHART RRDLQPDPEF DPICALFYCI SSDTPLPDTE KTELTGVIVI
DKDKTVTHQD IRSQTPLLIR SGITGLEVTY AADEKALFQE ITNIIKRYDP DILLGYEIQM
HSWGYLLQRA AALSVDLCQM ISRVPDDKIE NRFAAERDDY GSDTMSEINI VGRITLNLWR
IMRNEVALTN YTFENVSFHV LHQRFPLFTF RVLSDWFDNK TDLYRWKMVD HYVSRVRGNL
QMLEQLDLIG KTSEMARLFG IQFLHVLTRG SQYRVESMML RIAKPMNYIP VTPSIQQRSQ
MRAPQCVPLI MEPESRFYSN SVLVLDFQSL YPSIVIAYNY CFSTCLGHVE NLGKYDEFKF
GCTSLRVPPD LLYQIRHDVT VSPNGVAFVK PSVRKGVLPR MLEEILKTRL MVKQSMKSYK
QDRALSRMLN ARQLGLKLIA NVTFGYTAAN FSGRMPCIEV GDSIVHKARE TLERAIKLVN
DTKKWGARVV YGDTDSMFVL LKGATKEQSF KIGQEIAEAV TATNPRPVKL KFEKVYLPCV
LQTKKRYVGY MYETLDQKEP VFDAKGIETV RRDSCPAVSK ILERSLKLLF ETRDISLIKQ
YVQRQCMKLV EGKASIQDFI FAKEYRGSFS YRPGACVPAL ELTRKMLAYD RRSEPRVGER
VPYVIIYGTP GLPLIQLIRR PAEVLQDPTL RLNATYYITK QILPPLARIF SLIGIDVFSW
YQELPRIQKA TSSSRSELEG RKGTISQYFT TLHCPVCDDL TQHGICSKCR SQPQHVAIIL
NQEIRELERK QEQLIKICRN CTGSFDRHIP CVSLNCPVLF KLSRVNRELS KAPYLRQLLD
QF
